Such increase in local density of surface protein could explain the preferential binding of Lo cell poles to glass surfaces.
Bacterial adhesion to glass surfaces was studied using microscopic slides cleaned with ethanol and TFD4 detergent.
The derivatization process imparts a positive charge to glass surfaces, which allows DNA immobilization [ 5, 12– 12].
The pedestal surface was coated with casein to prevent α-actinin-coated beads from nonspecific binding to the glass surface.
Differences on adhesion to glass surface among mutans streptococci group were already observed [ 27].
The probes, which had a 3'-aminolink (3'-aminopropanol) modification for covalent binding to the glass slide surface [ 24], were purchased from Integrated DNA Technologies Inc. (Coralville, IA, USA).
This effect could also increase the possibility of catechol groups to generate strong bonding to the glass surfaces through the formation of hydrogen bonds to the hydroxyl groups of the glass surfaces, increasing the interfacial adhesion of the polymer.
To quantify the adhesive forces of the tripeptide sample to the glass surfaces, atomic force microscopy (AFM) was used.
The background br is an offset due mainly to unspecific binding of labeled CaM to the glass surface which was determined using a labeled CaM bound to a high affinity CKII(290 312)* peptide without a Cystein residue.
Here, BCML was used to pattern glass surfaces with gold nanoparticles (Au-NPs).
